Two long years in the South Korean military gave Eunyong Park time to change his mind and his career direction toward biology, a change that led to his winning this year’s $3,000 Kaluza prize for excellence in graduate research. Park won the ASCB Kaluza Prize, which is supported by Beckman Coulter, for his remarkable work at Harvard University deciphering the mechanisms of protein translocation in living cells. When cells make new proteins that are destined to reside in the membrane or enter the secretory pathway, they are threaded through channels in the endoplasmic reticulum (ER). The location of these channels deep inside the ER, which is deep inside the cell, make them difficult to study. Catching a protein in the act of translocation through the ER is an even more daunting challenge. Park developed new methods to examine these essential and specialized channels and even caught a structural snapshot of protein translocation.
Park grew up in Seoul, South Korea, where he earned a bachelor’s degree in chemical engineering at Seoul National University. After graduation, he was called up for military service required of all male South Koreans, Those two years, said Park, gave him plenty of time to think about what to do next. He decided to switch from chemical engineering to biology. He’d had a taste of biology in a few undergraduate courses and, soon after his discharge, he went for a master’s degree in biochemistry from his alma mater where he did his first research on protein biochemistry.
Park was fascinated by the subject and wanted to pursue protein biochemistry further, especially to understand the structure of membrane proteins. In 2006, he was accepted into a PhD program at Harvard and soon after into the lab of Tom Rappoport, who set him a challenge: Figure out a way to get at the structure of the translocation intermediate complex. It took him three years to develop workable methods to study the translocation channel in bacteria (SecY) that is equivalent to that of eukaryotes.
“I was trying everything that I could try. It was kind of lucky,” Park said. But then his project was scooped by another group. “We were kind of devastated,” Park recalled, but he quickly recovered, resolving to repurpose his innovative techniques. “We thought about how to use that method with other problems,” Park said, and the lab turned to elucidating how the translocating channel can prevent the passage of small molecules while continuing to translocate big polypeptide chains. Eventually Park was able to resolve the structure of the translocation channel SecY during initiation of translocation through cryo-electron microscopy (cryo-EM).
Now a postdoc in Roderick MacKinnon’s lab at the Rockefeller University, Park reports that he is thrilled to be finally learning proper x-ray crystallography, which he was unable to do during his PhD. “Roderick is a top membrane protein biologist and also a renowned structural biologist. I came here to learn more about structural biology,” Park said. “[Crystallography] is quite tedious but in the end you get the structure, and that’s really rewarding.”
Park is unruffled by the deliberate pace of long-term research projects but in his free time, he loves to escape the confines of the lab—and Manhattan—on hikes. He also loves the instant gratification of digital photography and plans to use part of the $3,000 Kaluza prize to buy a better camera.
About the Author:
Christina Szalinski is a science writer with a PhD in Cell Biology from the University of Pittsburgh.
